Her4 and Her2/neu Tyrosine Kinase Domains Dimerize and Activate in a Reconstituted in Vitro System

Gelijkaardige items

• Carboxyl Group Footprinting Mass Spectrometry and Molecular Dynamics Identify Key Interactions in the HER2-HER3 Receptor Tyrosine Kinase Interface
  door: Collier, Timothy S., et al.
  Gepubliceerd in: (2013)
• Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases
  door: Keppel, Theodore R., et al.
  Gepubliceerd in: (2017)
• Carboxyl-Group Footprinting Maps the Dimerization Interface and Phosphorylation-induced Conformational Changes of a Membrane-associated Tyrosine Kinase
  door: Zhang, Hao, et al.
  Gepubliceerd in: (2011)
• Rotational Coupling of the Transmembrane and Kinase Domains of the Neu Receptor Tyrosine Kinase
  door: Bell, Charlotte A., et al.
  Gepubliceerd in: (2000)
• Structural Details of an Oncogenic Dimer♦: Carboxyl Group Footprinting Mass Spectrometry and Molecular Dynamics Identify Key Interactions in the HER2-HER3 Receptor Tyrosine Kinase Interface
  Gepubliceerd in: (2013)